Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4WL79 (BGLH_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable beta-glucosidase H

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase H
Cellobiase H
Gentiobiase H
Gene names
Name:bglH
ORF Names:AFUA_6G14490
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length829 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Pathway

Glycan metabolism; cellulose degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Contains 1 PA14 domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 829829Probable beta-glucosidase H
PRO_0000394879

Regions

Domain391 – 535145PA14

Sites

Active site2251 By similarity

Amino acid modifications

Glycosylation131N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation4731N-linked (GlcNAc...) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Glycosylation6271N-linked (GlcNAc...) Potential
Glycosylation6641N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WL79 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 9FC9D770D59A9ED9

FASTA82990,990
        10         20         30         40         50         60 
MTPKFDIDYV LANITEDDKI ALLSGSDFWH THAIPKFNVP PIRTTDGPNG IRGTKFFAGV 

        70         80         90        100        110        120 
PAACLPCGTA LGATWDRDLL HQAGVLLGKE CLAKGAHCWL GPTINMQRSP LGGRGFESFA 

       130        140        150        160        170        180 
EDPHLSGIMA KSIILGCEST GVISTVKHYV GNDQEHERRA VDVLVTPRAL REIYLRPFQI 

       190        200        210        220        230        240 
VARDAHPGAL MTSYNKINGK HVVENPAMLD IVRKDWHWDP LIMSDWLGTY TTIDSLNAGL 

       250        260        270        280        290        300 
DLEMPGPTRY RGKYIESAMQ ARLIKQSTIS KRARKVLEFV ERASRAPVSA DETGRDFPED 

       310        320        330        340        350        360 
RALNRTLCAN SIVLLKNDGN LLPIPKTVKK IALIGSHVKT PAISGGGSAS LEPYYAVSLY 

       370        380        390        400        410        420 
DAVVEALPDA EILYEAGAYA HRMLPVIDRM LSNAVIHFYN EPPEKERTLL ATEPVVNTAF 

       430        440        450        460        470        480 
QLMDYNAPGL NRALFWATLI GEFTPDVSGL WDFGLTVFGT ATLFIDDEMV IDNATRQTRG 

       490        500        510        520        530        540 
TAFFGKGTVQ EVGQKQLTAG QTYKIRIEFG SANTSPMKAI GVVHFGGGAA HLGACLHMDP 

       550        560        570        580        590        600 
EQMVANAVRV AAEADYTIVC TGLNRDWESE GFDRPDMDLP PGIDALISSV LDVAADRTVI 

       610        620        630        640        650        660 
VNQSGTPVTM PWAHRARGIV QAWYGGNETG HGIADVLFGD VNPSGKLPLS WPADVRHNPT 

       670        680        690        700        710        720 
YLNNMSVGGR MLYGEDVYIG YRFYEKVGRE VLFPFGHGLS YTTFHVSPEA TVSPIVFSSD 

       730        740        750        760        770        780 
SPPTATVLVK NTGPMAGAQT LQLYIAAPNS ATPRPVKELH GFTKVFLQSG EERSVSIHID 

       790        800        810        820 
RYATSFWDEI EDMWKSEEGV YQVLIGTSSQ EIVSRGEFRV EQTRYWRGV 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000006 Genomic DNA. Translation: EAL89285.1.
RefSeqXP_751323.1. XM_746230.1.

3D structure databases

ProteinModelPortalQ4WL79.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00002146; CADAFUAP00002146; CADAFUAG00002146.
GeneID3508640.
KEGGafm:AFUA_6G14490.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK01238.
OMAGCESTGV.
OrthoDBEOG7H799Q.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
IPR011658. PA14.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SMARTSM00758. PA14. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
ProtoNetSearch...

Entry information

Entry nameBGLH_ASPFU
AccessionPrimary (citable) accession number: Q4WL79
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries